ID V8NB97_OPHHA Unreviewed; 501 AA.
AC V8NB97;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
DE Flags: Fragment;
GN ORFNames=L345_14746 {ECO:0000313|EMBL:ETE59524.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE59524.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE59524.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE59524.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000398};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000256|ARBA:ARBA00005465}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE59524.1}.
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DR EMBL; AZIM01005517; ETE59524.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NB97; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742:SF355; AMINE OXIDASE; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Antibiotic {ECO:0000256|ARBA:ARBA00023022};
KW Antimicrobial {ECO:0000256|ARBA:ARBA00023022};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemolysis {ECO:0000256|ARBA:ARBA00022735};
KW Hemostasis impairing toxin {ECO:0000256|ARBA:ARBA00023240};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT DOMAIN 52..484
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 501
FT /evidence="ECO:0000313|EMBL:ETE59524.1"
SQ SEQUENCE 501 AA; 57294 MW; 54F9906937206246 CRC64;
MTIWVSENHA NEQEDWMKCF EDPNYEELLN IARNGLEKTS EPKKIVIVGA GISGLTAAKL
LKDAGHQVHI LEASNRIGGR INTHREKDWY VELGAMRLPK AHRICREYIK KFNLSLNPFV
LSNKNAWYLF RNRRERVSAV NENPNVFGYP MRNTELGKSA EELYKSTLDR TTKNCTRLKM
KYDSYSTKEY LIKEGNLSSG AVAMIGDLFN KGVEYYVSFF TSVLNYITFS DENGFEEITG
GFDQLPNSFY QEMSRIIHLN SRVEKIIRSG KKVKVFFHKE DEDDSSLLIV DYVLVTATAK
ATRLIKFQPP LSHLKAYALY SLHYTSATKV VLVCTDKFWE REGIRGGVSM TDNPTRLVSY
PSHDFPGGLG VLLVSYTVDD DADFFVPLSD DECLDVVMND LSKIHNISKI YLESVCNRHV
IQKWALDKFS MGAFSFPTPY QYSFFIKALF QNEGRVYFAG EHTTYPFAWI DSAMKSAIRA
ASNIHLNAHK SISQELKESA W
//
